A BK (Slo1) channel journey from molecule to physiology

Autores
Contreras, Gustavo F.; Castillo, Karen; Enrique, Nicolás Jorge; Carrasquel Ursulaez, Willy; Castillo, Juan Pablo; Milesi, Verónica; Neely, Alan; Alvarez, Osvaldo; Ferreira, Gonzalo; Gonzalez, Carlos; Latorre, Ramón
Año de publicación
2013
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and non-neuronal cells and tissues. Through negative feedback between intracellular Ca2+ and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel ́ subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca2+ sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression.
Facultad de Ciencias Exactas
Materia
Ciencias Exactas
Auxiliary subunits
BK channels
Diseases
Slo1
Smooth muscle
Voltage sensor
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/85241
Acceder
id SEDICI_09e518065c1c40cde980657d1b167d34
oai_identifier_str oai:sedici.unlp.edu.ar:10915/85241
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling A BK (Slo1) channel journey from molecule to physiologyContreras, Gustavo F.Castillo, KarenEnrique, Nicolás JorgeCarrasquel Ursulaez, WillyCastillo, Juan PabloMilesi, VerónicaNeely, AlanAlvarez, OsvaldoFerreira, GonzaloGonzalez, CarlosLatorre, RamónCiencias ExactasAuxiliary subunitsBK channelsDiseasesSlo1Smooth muscleVoltage sensorCalcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and non-neuronal cells and tissues. Through negative feedback between intracellular Ca<SUP>2+</SUP> and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel ́ subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca<SUP>2+</SUP> sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression.Facultad de Ciencias Exactas2013info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/85241enginfo:eu-repo/semantics/altIdentifier/issn/1933-6950info:eu-repo/semantics/altIdentifier/doi/10.4161/chan.26242info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:34Zoai:sedici.unlp.edu.ar:10915/85241Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:34.935SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv A BK (Slo1) channel journey from molecule to physiology
title A BK (Slo1) channel journey from molecule to physiology
spellingShingle A BK (Slo1) channel journey from molecule to physiology
Contreras, Gustavo F.
Ciencias Exactas
Auxiliary subunits
BK channels
Diseases
Slo1
Smooth muscle
Voltage sensor
title_short A BK (Slo1) channel journey from molecule to physiology
title_full A BK (Slo1) channel journey from molecule to physiology
title_fullStr A BK (Slo1) channel journey from molecule to physiology
title_full_unstemmed A BK (Slo1) channel journey from molecule to physiology
title_sort A BK (Slo1) channel journey from molecule to physiology
dc.creator.none.fl_str_mv Contreras, Gustavo F.
Castillo, Karen
Enrique, Nicolás Jorge
Carrasquel Ursulaez, Willy
Castillo, Juan Pablo
Milesi, Verónica
Neely, Alan
Alvarez, Osvaldo
Ferreira, Gonzalo
Gonzalez, Carlos
Latorre, Ramón
author Contreras, Gustavo F.
author_facet Contreras, Gustavo F.
Castillo, Karen
Enrique, Nicolás Jorge
Carrasquel Ursulaez, Willy
Castillo, Juan Pablo
Milesi, Verónica
Neely, Alan
Alvarez, Osvaldo
Ferreira, Gonzalo
Gonzalez, Carlos
Latorre, Ramón
author_role author
author2 Castillo, Karen
Enrique, Nicolás Jorge
Carrasquel Ursulaez, Willy
Castillo, Juan Pablo
Milesi, Verónica
Neely, Alan
Alvarez, Osvaldo
Ferreira, Gonzalo
Gonzalez, Carlos
Latorre, Ramón
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Auxiliary subunits
BK channels
Diseases
Slo1
Smooth muscle
Voltage sensor
topic Ciencias Exactas
Auxiliary subunits
BK channels
Diseases
Slo1
Smooth muscle
Voltage sensor
dc.description.none.fl_txt_mv Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and non-neuronal cells and tissues. Through negative feedback between intracellular Ca<SUP>2+</SUP> and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel ́ subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca<SUP>2+</SUP> sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression.
Facultad de Ciencias Exactas
description Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and non-neuronal cells and tissues. Through negative feedback between intracellular Ca<SUP>2+</SUP> and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel ́ subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca<SUP>2+</SUP> sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/review
info:eu-repo/semantics/publishedVersion
Revision
http://purl.org/coar/resource_type/c_dcae04bc
info:ar-repo/semantics/resenaArticulo
format review
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/85241
url http://sedici.unlp.edu.ar/handle/10915/85241
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1933-6950
info:eu-repo/semantics/altIdentifier/doi/10.4161/chan.26242
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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